Recombinant Human ARF4 Protein

Name: Recombinant Human ARF4 Protein
Brand: Beta LifeScience
SKU: BLA-12197P
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Host Species	Human
Accession	P18085
Synonym	ADP ribosylation factor 2 ADP ribosylation factor 4 ADP-ribosylation factor 4 ARF2 ARF4 ARF4_HUMAN
Description	Recombinant Human ARF4 Protein was expressed in E.coli. It is a Full length protein
Source	E.coli
AA Sequence	MGSSHHHHHHSSGLVPRGSHMGSHMGLTISSLFSRLFGKKQMRILMVGLD AAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDRIRP LWKHYFQNTQGLIFVVDSNDRERIQEVADELQKMLLVDELRDAVLLLFAN KQDLPNAMAISEMTDKLGLQSLRNRTWYVQATCATQGTGLYEGLDWLSNE LSKR
Molecular Weight	23 kDa including tags
Purity	Greater than 95% SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Liquid Solution
Stability	The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution	See related COA
Unit Definition	For Research Use Only
Storage Buffer	Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycle.

Target Details

Target Function	GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular Location	Golgi apparatus. Membrane; Lipid-anchor.
Protein Families	Small GTPase superfamily, Arf family
Database References	HGNC: 655 OMIM: 601177 KEGG: hsa:378 STRING: 9606.ENSP00000306010 UniGene: Hs.652183

Gene Functions References

In summary, the authors show here that hepatitis C virus infection is associated with an upregulation of ARF4, which promotes hepatitis C virus replication. Upon hepatitis C virus infection, CREB3 was redistributed to nucleus and activated ARF4 transcription. PMID: 28840565
found ADP-ribosylation factor (ARF) 4 is one of the putative target genes of Mir-221, and the direct binding relationship was further confirmed by dual-luciferase reporter assay. PMID: 28057486
Data suggest that, when compared to intestinal epithelial cells (IECs) from germ-free mice, IECs from mice with commensal bacteria exhibit increased expression of microRNA-21-5p; up-regulation of expression of microRNA-21-5p appears to increase IEC permeability and up-regulates ADP ribosylation factor 4 (Arf4/ARF4) in mouse and human cells. PMID: 28760826
ARF1+ARF4 are required for integrity of recycling endosomes but are involved in distinct transport pathways: the pair regulates retrograde transport from endosomes to the TGN. PMID: 23783033
A CREB3-ARF4 signalling cascade may be part of a Golgi stress response set in motion by stimuli compromising Golgi capacity. PMID: 24185178
a crucial role for class II Arf proteins (Arf4 and Arf5) in the dengue flavivirus life cycle PMID: 22105072
The lipid droplets deposition and the cellular triacylglycerol content are significantly increased by siRNA-mediated depletion of Arf4. PMID: 22185782
sLZIP-regulated ARF4 expression in response to phorbol 12-myristate 13-acetate is involved in breast cancer cell migration. PMID: 22004728
Arf4 regulates PLA2G6-A activity together with Arf1; and gene silencing of Arf4 was shown to alter cytosolic coat protein I subunit recruitment to the early secretory pathway. PMID: 20881058
ARF4 is a critical molecule that directly regulates cellular phospholipase D2 activity and this ARF4-mediated PLD2 activation stimulates AP-1-dependent transcription in the EGF-induced cellular response PMID: 12446727
ARF4L occurred on the plasma membrane after binding to GTP and into endosomes while binding to GDP; the inactive form of ARF4L causes localization of transferrin receptors to the endosomes while the active form causes transport to the plasma membrane. PMID: 15049518
ARF4 participates in the regulation of glioblastoma apoptosis through the inhibition of stress-mediated apoptotic signals PMID: 19041174

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.